ID   DHAA_RHORH              Reviewed;         293 AA.
AC   P0A3G2; Q53042;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Haloalkane dehalogenase;
DE            EC=3.8.1.5;
GN   Name=dhaA;
OS   Rhodococcus rhodochrous.
OG   Plasmid pRTL1.
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=1829;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NCIMB 13064;
RX   PubMed=9025284; DOI=10.1099/00221287-143-1-109;
RA   Kulakova A.N., Larkin M.J., Kulakov L.A.;
RT   "The plasmid-located haloalkane dehalogenase gene from Rhodococcus
RT   rhodochrous NCIMB 13064.";
RL   Microbiology 143:109-115(1997).
CC   -!- FUNCTION: Catalyzes hydrolytic cleavage of carbon-halogen bonds in
CC       halogenated aliphatic compounds, leading to the formation of the
CC       corresponding primary alcohols, halide ions and protons. Expresses
CC       halogenase activity against 1-chloroalkanes of chain length C3 to C10,
CC       and also shows a very weak activity with 1,2-dichloroethane.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-haloalkane + H2O = a halide anion + a primary alcohol +
CC         H(+); Xref=Rhea:RHEA:19081, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15734, ChEBI:CHEBI:16042, ChEBI:CHEBI:18060; EC=3.8.1.5;
CC   -!- PATHWAY: Xenobiotic degradation; haloalkane degradation.
CC   -!- SUBUNIT: Monomer.
CC   -!- INDUCTION: By 1-haloalkanes.
CC   -!- SIMILARITY: Belongs to the haloalkane dehalogenase family. Type 2
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AF060871; AAC15838.1; -; Genomic_DNA.
DR   PDB; 2V9Z; X-ray; 3.00 A; A=1-293.
DR   PDB; 3FBW; X-ray; 1.23 A; A=1-293.
DR   PDB; 3RK4; X-ray; 1.31 A; A=1-293.
DR   PDB; 3SK0; X-ray; 1.78 A; A=1-293.
DR   PDB; 4E46; X-ray; 1.26 A; A=1-293.
DR   PDB; 4F5Z; X-ray; 1.20 A; A=1-293.
DR   PDB; 4F60; X-ray; 1.45 A; A=1-293.
DR   PDB; 4FWB; X-ray; 1.26 A; A=4-293.
DR   PDB; 4WCV; X-ray; 1.69 A; A=1-293.
DR   PDB; 5FLK; X-ray; 0.99 A; A=1-293.
DR   PDB; 5UXZ; X-ray; 1.92 A; A/B=4-290.
DR   PDB; 5UY1; X-ray; 1.35 A; A/B=4-290.
DR   PDB; 5VNP; X-ray; 2.23 A; A/B=4-293.
DR   PDB; 6SP5; X-ray; 1.60 A; A/B=3-293.
DR   PDB; 6SP8; X-ray; 1.55 A; A/B=3-293.
DR   PDB; 6TY7; X-ray; 1.50 A; A/B=1-293.
DR   PDB; 6XT8; X-ray; 1.70 A; A/B/C/D=1-293.
DR   PDB; 6XTC; X-ray; 2.54 A; A/B/C/D=1-293.
DR   PDB; 7O3O; X-ray; 1.25 A; A=1-293.
DR   PDB; 7O8B; X-ray; 1.75 A; A=4-293.
DR   PDBsum; 2V9Z; -.
DR   PDBsum; 3FBW; -.
DR   PDBsum; 3RK4; -.
DR   PDBsum; 3SK0; -.
DR   PDBsum; 4E46; -.
DR   PDBsum; 4F5Z; -.
DR   PDBsum; 4F60; -.
DR   PDBsum; 4FWB; -.
DR   PDBsum; 4WCV; -.
DR   PDBsum; 5FLK; -.
DR   PDBsum; 5UXZ; -.
DR   PDBsum; 5UY1; -.
DR   PDBsum; 5VNP; -.
DR   PDBsum; 6SP5; -.
DR   PDBsum; 6SP8; -.
DR   PDBsum; 6TY7; -.
DR   PDBsum; 6XT8; -.
DR   PDBsum; 6XTC; -.
DR   PDBsum; 7O3O; -.
DR   PDBsum; 7O8B; -.
DR   AlphaFoldDB; P0A3G2; -.
DR   SMR; P0A3G2; -.
DR   ESTHER; rhoso-halo1; Haloalkane_dehalogenase-HLD2.
DR   BRENDA; 3.8.1.5; 5395.
DR   SABIO-RK; P0A3G2; -.
DR   UniPathway; UPA00007; -.
DR   EvolutionaryTrace; P0A3G2; -.
DR   GO; GO:0018786; F:haloalkane dehalogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   HAMAP; MF_01231; Haloalk_dehal_type2; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   InterPro; IPR023594; Haloalkane_dehalogenase_2.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Detoxification; Hydrolase; Plasmid.
FT   CHAIN           1..293
FT                   /note="Haloalkane dehalogenase"
FT                   /id="PRO_0000216775"
FT   DOMAIN          34..158
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        106
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   STRAND          13..17
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          20..28
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          30..32
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          35..38
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           45..48
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   TURN            49..51
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           52..55
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   TURN            56..58
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           81..94
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           106..118
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          123..130
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:3RK4"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           146..152
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          154..156
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           157..162
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   TURN            163..165
FT                   /evidence="ECO:0007829|PDB:6XTC"
FT   HELIX           167..170
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           172..175
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          177..179
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           183..190
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           191..193
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           196..199
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           200..208
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           216..231
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          236..243
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          245..247
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           249..258
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   STRAND          262..272
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           274..277
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           279..289
FT                   /evidence="ECO:0007829|PDB:5FLK"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:5FLK"
SQ   SEQUENCE   293 AA;  33246 MW;  2B637C53E36BE9F3 CRC64;
     MSEIGTGFPF DPHYVEVLGE RMHYVDVGPR DGTPVLFLHG NPTSSYLWRN IIPHVAPSHR
     CIAPDLIGMG KSDKPDLDYF FDDHVRYLDA FIEALGLEEV VLVIHDWGSA LGFHWAKRNP
     ERVKGIACME FIRPIPTWDE WPEFARETFQ AFRTADVGRE LIIDQNAFIE GALPKCVVRP
     LTEVEMDHYR EPFLKPVDRE PLWRFPNELP IAGEPANIVA LVEAYMNWLH QSPVPKLLFW
     GTPGVLIPPA EAARLAESLP NCKTVDIGPG LHYLQEDNPD LIGSEIARWL PAL